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Accession Type:
Network
AMPAR_traff_
model0
Shared_Object_
AMPAR_traff_
model0
CaMKII
CaM
PP1
 Molecule
 Enzyme
 Reaction
PP2B
PP1_PSD
PKA
AC
AMPAR
AMPAR_memb

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Enzyme List for pathway PP1 (Pathway Number 237)

 Molecule Name/
Site Name
Km (uM) kcat (1/s)Ratio
(k2/k3)
Enzyme TypeSubstrate Product
1 Enzyme Activity:
Deph-thr286

Enzyme Molecule:
PP1-active
5.099052.54explicit E-S complex
  • CaMKII-thr286*-C
    aM

  • CaMKII-CaM
    2 Enzyme Activity:
    Deph-thr286b

    Enzyme Molecule:
    PP1-active
    5.099052.54explicit E-S complexCaMKII-thr286
    CaMKII
    3 Enzyme Activity:
    Deph-thr286c

    Enzyme Molecule:
    PP1-active
    5.099052.54explicit E-S complexCaMKII***
    CaMK-thr305
    4 Enzyme Activity:
    Deph-thr305

    Enzyme Molecule:
    PP1-active
    5.099052.54explicit E-S complexCaMKII***
    CaMKII-thr286
    5 Enzyme Activity:
    Deph-thr305a

    Enzyme Molecule:
    PP1-active
    5.099052.54explicit E-S complexCaMK-thr305
    CaMKII
    6 Enzyme Activity:
    PP2A-dephosph-I1

    Enzyme Molecule:
    PP2A
    15.999924.1667explicit E-S complexI1*
    I1
      PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6
    7 Enzyme Activity:

    PP2A-dephosph-I1
    _
    PSD

    Enzyme Molecule:
    PP2A
    15.999924.1667explicit E-S complexI1*
    I1
      PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6
    8 Enzyme Activity:
    PP2A-dephosph-PP
    1-I*

    Enzyme Molecule:
    PP2A
    15.999924.1667explicit E-S complexPP1-I1*
    PP1-I1
      k1 changed from 3.3e-6 to 6.6e-6
    9 Enzyme Activity:

    PP2A-dephosph-PP
    1-I*_
    PSD

    Enzyme Molecule:
    PP2A
    15.999924.1667explicit E-S complexPP1-I1*
    PP1-I1
      k1 changed from 3.3e-6 to 6.6e-6


    Pathway Details   Molecule List  Enzyme List   Reaction List  


    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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